5nff
From Proteopedia
Crystal structure of GP1 receptor binding domain from Morogoro virus
Structural highlights
FunctionC6ZK00_MOPEI Forms the virion spikes together with glycoprotein G2. The glycoprotein spike trimers are connected to the underlying matrix. Interacts with the host receptor leading to virus endocytosis.[HAMAP-Rule:MF_04084] Forms the virion spikes together with glycoprotein G1. The glycoprotein spike trimers are connected to the underlying matrix. Class I viral fusion protein that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversible conformational changes induced by acidification.[HAMAP-Rule:MF_04084] Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C). Helps to stabilize the spike complex in its native conformation. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of G1 and G2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion.[HAMAP-Rule:MF_04084] Publication Abstract from PubMedCell entry of many enveloped viruses occurs by engagement with cellular receptors, followed by internalization into endocytic compartments and pH-induced membrane fusion. A previously unnoticed step of receptor switching was found to be critical during cell entry of two devastating human pathogens: Ebola and Lassa viruses. Our recent studies revealed the functional role of receptor switching to LAMP1 for triggering membrane fusion by Lassa virus and showed the involvement of conserved histidines in this switching, suggesting that other viruses from this family may also switch to LAMP1. However, when we investigated viruses that are genetically close to Lassa virus, we discovered that they cannot bind LAMP1. A crystal structure of the receptor-binding module from Morogoro virus revealed structural differences that allowed mapping of the LAMP1 binding site to a unique set of Lassa residues not shared by other viruses in its family, illustrating a key difference in the cell-entry mechanism of Lassa virus that may contribute to its pathogenicity. Mapping of the Lassa virus LAMP1 binding site reveals unique determinants not shared by other old world arenaviruses.,Israeli H, Cohen-Dvashi H, Shulman A, Shimon A, Diskin R PLoS Pathog. 2017 Apr 27;13(4):e1006337. doi: 10.1371/journal.ppat.1006337., eCollection 2017 Apr. PMID:28448640[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
| ||||||||||||||||||||
